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Journal of Virology, August 2006, p. 8190-8198, Vol. 80, No. 16
0022-538X/06/$08.00+0     doi:10.1128/JVI.00504-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Hydrophobic {alpha}-Helices 1 and 2 of Herpes Simplex Virus gH Interact with Lipids, and Their Mimetic Peptides Enhance Virus Infection and Fusion

Tatiana Gianni,1 Romana Fato,2 Christian Bergamini,2 Giorgio Lenaz,2 and Gabriella Campadelli-Fiume1*

Department of Experimental Pathology, Section on Microbiology and Virology,1 Department of Biochemistry "G. Moruzzi," Alma Mater Studiorum—University of Bologna, Via San Giacomo, 12, and Via Irnerio 48, 40126 Bologna, Italy2

Received 10 March 2006/ Accepted 30 May 2006

Entry of herpes simplex virus into cells occurs by fusion and requires four glycoproteins. gD serves as the receptor binding glycoprotein. Of the remaining glycoproteins, gH carries structural and functional elements typical of class 1 fusion glycoproteins, in particular {alpha}-helix 1 ({alpha}-H1), with properties of a candidate fusion peptide, and two heptad repeats. Here, we characterized {alpha}-H2 and compared it to {alpha}-H1. {alpha}-H2 (amino acids 513 to 531) is of lower hydrophobicity than {alpha}-H1. Its deletion or mutation decreased virus infection and cell fusion. Its replacement with heterologous fusion peptides did not rescue infection and cell fusion beyond the levels exhibited by the {alpha}-H2-deleted gH. This contrasts with {alpha}-H1, which cannot be deleted and can be functionally replaced with heterologous fusion peptides (T. Gianni et al., J. Virol. 79:2931-2940, 2005). Synthetic peptides mimicking {alpha}-H1 and {alpha}-H2 induced fusion of nude lipid vesicles. Importantly, they increased infection of herpes simplex virus, pseudorabies virus, bovine herpesvirus 1, and vesicular stomatitis virus. The {alpha}-H1 mimetic peptide was more effective than the {alpha}-H2 peptide. Consistent with the findings that gH carries membrane-interacting segments, a soluble form of gH, but not of gD or gB, partitioned with lipid vesicles. Current findings highlight that {alpha}-H2 is an important albeit nonessential region for virus entry and fusion. {alpha}-H1 and {alpha}-H2 share the ability to target the membrane lipids; they contribute to virus entry and fusion, possibly by destabilizing the membranes. However, {alpha}-H2 differs from {alpha}-H1 in that it is of lower hydrophobicity and cannot be replaced with heterologous fusion peptides.

* Corresponding author. Mailing address: Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12-40126 Bologna, Italy. Phone: 39 051 2094733/2094734. Fax: 39 051 2094735. E-mail: gabriella.campadelli{at}unibo.it.

Journal of Virology, August 2006, p. 8190-8198, Vol. 80, No. 16
0022-538X/06/$08.00+0     doi:10.1128/JVI.00504-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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